protein polymerization
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Author(s):  
Xin Wu ◽  
Wei Yang ◽  
Xiao-Hua Gou ◽  
Xiao-Yun Xu ◽  
Na Lu ◽  
...  

IntroductionThe present study aimed to investigate the differences in the proteomic expression between uncomplicated parapneumonic pleural effusion (UPPE) and complicated parapneumonic pleural effusion (CPPE).Material and methodsThere were 10 patients with UPPE and 10 patients with CPPE. These patients were combined due to the complication of pleural effusion and further divided into group A and group B. An LC-MS analysis was conducted with the extraction of high-abundance proteins, and proteins with 1.5-fold or higher difference multiples were identified as differential proteins. Then, gene ontology (GO) and KEGG analyses were conducted on the differential proteins between the groups.ResultsCompared with the UPPE group, there were 38 upregulated proteins and 29 downregulated proteins in the CPPE group. The GO analysis revealed that the CPPE group had enhanced expressions in monosaccharide biosynthesis, glucose catabolism, fructose-6-phosphate glycolysis, glucose-6-phosphate glycolysis, and NADH regeneration as well as reduced expressions in fibrinogen complexes, protein polymerization, and coagulation. Moreover, the KEGG analysis showed that the CPPE group had enhanced expressions in amino acid synthesis, the HIF-1 signalling pathway, and glycolysis/glyco-isogenesis and decreased expressions in platelet activation and complement activation.ConclusionsIn pleural effusion in patients with CPPE, there are enhanced expressions of proteins concerning glucose and amino acid metabolism, NADH regeneration, and HIF-1 signalling pathways together with decreased expressions of proteins concerning protein polymerization, blood coagulation, platelet activation, and complement activation.


Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1717
Author(s):  
Elaine Berger Ceresino ◽  
Eva Johansson ◽  
Hélia Harumi Sato ◽  
Tomás S. Plivelic ◽  
Stephen A. Hall ◽  
...  

This study addresses an innovative approach to generate aerated foods with appealing texture through the utilization of lupin protein isolate (LPI) in combination with edible fats. We show the impact of transglutaminases (TGs; SB6 and commercial), glycerol (Gly), soy lecithin (Lec) and linoleic acid (LA) on the micro- and nanostructure of health promoting solid foods created from LPI and fats blends. 3-D tomographic images of LPI with TG revealed that SB6 contributed to an exceptional bubble spatial organization. The inclusion of Gly and Lec decreased protein polymerization and also induced the formation of a porous layered material. LA promoted protein polymerization and formation of homogeneous thick layers in the LPI matrix. Thus, the LPI is a promising protein resource which when in blend with additives is able to create diverse food structures. Much focus has been placed on the great foamability of LPI and here we show the resulting microstructure of LPI foams, and how these were improved with addition of TGs. New food applications for LPI can arise with the addition of food grade dispersant Lec and essential fatty-acid LA, by improved puffiness, and their contributing as replacer of chemical leavening additives in gluten-free products.


LWT ◽  
2020 ◽  
Vol 133 ◽  
pp. 109894
Author(s):  
Meng Wang ◽  
Zizhu Zhao ◽  
Meng Niu ◽  
Siming Zhao ◽  
Caihua Jia ◽  
...  

Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 555 ◽  
Author(s):  
Margarita Villar ◽  
Iván Pacheco ◽  
Octavio Merino ◽  
Marinela Contreras ◽  
Lourdes Mateos-Hernández ◽  
...  

Ticks are obligate hematophagous arthropods and vectors of pathogens affecting human and animal health worldwide. Cement is a complex protein polymerization substance secreted by ticks with antimicrobial properties and a possible role in host attachment, sealing the feeding lesion, facilitating feeding and pathogen transmission, and protection from host immune and inflammatory responses. The biochemical properties of tick cement during feeding have not been fully characterized. In this study, we characterized the proteome of Rhipicephalus microplus salivary glands (sialome) and cement (cementome) together with their physicochemical properties at different adult female parasitic stages. The results showed the combination of tick and host derived proteins and other biomolecules such as α-Gal in cement composition, which varied during the feeding process. We propose that these compounds may synergize in cement formation, solidification and maintenance to facilitate attachment, feeding, interference with host immune response and detachment. These results advanced our knowledge of the complex tick cement composition and suggested that tick and host derived compounds modulate cement properties throughout tick feeding.


Author(s):  
Akin Nihat ◽  
TzeHow Mok ◽  
John Collinge

Prion diseases are fatal neurodegenerative conditions that may arise sporadically or be inherited or acquired by environmental exposure to infectious prions—transmissible agents composed of multimeric assemblies of misfolded protein. The core clinical features are progressive cognitive decline, accompanied with ataxia, myoclonus, and pyramidal or extra-pramidal motor signs. While the most common form—sporadic Creutzfeldt–Jakob disease—is generally rapidly progressive over weeks or months, inherited prion diseases can span many years, with diverse clinical features readily mimicking other neurodegenerative diseases. Psychiatric features, including agitation, anxiety, depression, hallucinations, and behavioural disturbances, are common in the early stages. Diagnosis can usually be made with confidence by the combination of clinical criteria, diffusion-weighted magnetic resonance imaging, electroencephalogram, and specialized cerebrospinal fluid analysis. Inherited prion disease can be confirmed with prion protein gene analysis, which should be considered in all early-onset dementing and ataxic conditions. It is now becoming clear that the fundamental molecular pathogenesis—seeded protein polymerization—is relevant to other neurodegenerative diseases, notably Alzheimer’s disease.


2020 ◽  
Vol 305 ◽  
pp. 125500 ◽  
Author(s):  
Ting Liu ◽  
Meng Niu ◽  
Gary G. Hou

2019 ◽  
Vol 299 ◽  
pp. 125132 ◽  
Author(s):  
Mohd Asraf Mohd Zainudin ◽  
Mahesha M. Poojary ◽  
Sisse Jongberg ◽  
Marianne N. Lund

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